TY - JOUR
T1 - Structural Characterization of N-Linked Glycans in the Receptor Binding Domain of the SARS-CoV-2 Spike Protein and their Interactions with Human Lectins
AU - Lenza, Maria Pia
AU - Oyenarte, Iker
AU - Diercks, Tammo
AU - Quintana, Jon Imanol
AU - Gimeno, Ana
AU - Coelho, Helena
AU - Diniz, Ana
AU - Peccati, Francesca
AU - Delgado, Sandra
AU - Bosch, Alexandre
AU - Valle, Mikel
AU - Millet, Oscar
AU - Abrescia, Nicola G. A.
AU - Palazón, Asís
AU - Marcelo, Filipa
AU - Jiménez-Osés, Gonzalo
AU - Jiménez-Barbero, Jesús
AU - Ardá, Ana
AU - Ereño-Orbea, June
N1 - info:eu-repo/grantAgreement/WT/Physiological Sciences/095700
ERC‐2017‐AdG,
788143‐RECGLYCANMR
grant 200077
grant RTI2018‐094751‐B‐C21
GC2018‐098996‐B‐I00
RTI2018‐099592‐B‐C22
RTI2018‐101269‐B‐I00
SEV‐2016‐0644
IF/00780/2015
PTDC/BIA‐MIB/31028/2017
UCIBIO UIDB/04378/2020
Infrastructure project 22161
PD/BD/142847/2018
PY - 2020/12/21
Y1 - 2020/12/21
N2 - The glycan structures of the receptor binding domain of the SARS-CoV2 spike glycoprotein expressed in human HEK293F cells have been studied by using NMR. The different possible interacting epitopes have been deeply analysed and characterized, providing evidence of the presence of glycan structures not found in previous MS-based analyses. The interaction of the RBD 13C-labelled glycans with different human lectins, which are expressed in different organs and tissues that may be affected during the infection process, has also been evaluated by NMR. In particular, 15N-labelled galectins (galectins-3, -7 and -8 N-terminal), Siglecs (Siglec-8, Siglec-10), and C-type lectins (DC-SIGN, MGL) have been employed. Complementary experiments from the glycoprotein perspective or from the lectin's point of view have permitted to disentangle the specific interacting epitopes in each case. Based on these findings, 3D models of the interacting complexes have been proposed.
AB - The glycan structures of the receptor binding domain of the SARS-CoV2 spike glycoprotein expressed in human HEK293F cells have been studied by using NMR. The different possible interacting epitopes have been deeply analysed and characterized, providing evidence of the presence of glycan structures not found in previous MS-based analyses. The interaction of the RBD 13C-labelled glycans with different human lectins, which are expressed in different organs and tissues that may be affected during the infection process, has also been evaluated by NMR. In particular, 15N-labelled galectins (galectins-3, -7 and -8 N-terminal), Siglecs (Siglec-8, Siglec-10), and C-type lectins (DC-SIGN, MGL) have been employed. Complementary experiments from the glycoprotein perspective or from the lectin's point of view have permitted to disentangle the specific interacting epitopes in each case. Based on these findings, 3D models of the interacting complexes have been proposed.
KW - glycan
KW - lectin
KW - molecular recognition
KW - receptor binding domain
KW - SARS-CoV2
UR - http://www.scopus.com/inward/record.url?scp=85092927434&partnerID=8YFLogxK
U2 - 10.1002/anie.202011015
DO - 10.1002/anie.202011015
M3 - Article
C2 - 32915505
AN - SCOPUS:85092927434
SN - 1433-7851
JO - Angewandte Chemie - International Edition
JF - Angewandte Chemie - International Edition
ER -